Description
Title: Structural Proteomics for Metal Ion/Protein Binding Studies Using Mass Spectrometry
Abstract: Many proteins’ biological and physiological processes depend on metal ions. The study of protein and metal ion interactions is now being done using the rapidly expanding field of structural proteomics, which is based on mass spectrometry (MS). Native MS provides details on the stoichiometry of metal binding. With the help of MS and fingerprinting techniques, such as “fast photochemical oxidation of proteins” (FPOP), targeted amino-acid labeling, and hydrogen/deuterium exchange (HDX), binding sites and regions undergoing conformational changes can be found. Binding stoichiometry, affinity, and binding order can be determined using MS-based titration techniques, such as “protein-ligand interactions by mass spectrometry, titration, and HD exchange” (PLIMSTEX) and “ligand titration, fast photochemical oxidation of proteins, and mass spectrometry” (LITPOMS). This article discusses these MS-based structural proteomics methods, their applications to address issues with metal ion protein interactions, their drawbacks, and recent and future developments. This review serves as both a demonstration of these tools’ abilities and an introduction to broader applications that address other problems.
Keywords: mass spectrometry-based structural proteomics; HDX; FPOP; targeted amino-acid labeling; native MS; metal ion/protein interaction; binding site; binding affinity; stoichiometry; conformational change
Paper Quality: SCOPUS / Web of Science Level Research Paper
Subject: Biomolecules
Writer Experience: 20+ Years
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